1OXJ

Crystal structure of the Smaug RNA binding domain

Summary for 1OXJ

• Entry DOI: 10.2210/pdb1oxj/pdb
• Descriptor: RNA-binding protein Smaug (2 entities in total)
• Functional Keywords: sam domain, phat domain, rna-binding protein, rna binding protein
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Cytoplasm: Q23972
• Total number of polymer chains: 1
• Total formula weight: 19675.97

Authors

Green, J.B.,Gardner, C.D.,Wharton, R.P.,Aggarwal, A.K. (deposition date: 2003-04-02, release date: 2003-07-08, Last modification date: 2024-02-14)

Primary citation

Green, J.B.,Gardner, C.D.,Wharton, R.P.,Aggarwal, A.K.
RNA recognition via the SAM domain of Smaug.
Mol.Cell, 11:1537-1548, 2003

PubMed Abstract: The Nanos protein gradient in Drosophila, required for proper abdominal segmentation, is generated in part via translational repression of its mRNA by Smaug. We report here the crystal structure of the Smaug RNA binding domain, which shows no sequence homology to any previously characterized RNA binding motif. The structure reveals an unusual makeup in which a SAM domain, a common protein-protein interaction module, is affixed to a pseudo-HEAT repeat analogous topology (PHAT) domain. Unexpectedly, we find through a combination of structural and genetic analysis that it is primarily the SAM domain that interacts specifically with the appropriate nanos mRNA regulatory sequence. Therefore, in addition to their previously characterized roles in protein-protein interactions, some SAM domains play crucial roles in RNA binding.

PubMed: 12820967
DOI: 10.1016/S1097-2765(03)00178-3

Experimental method

X-RAY DIFFRACTION (1.8 Å)